Version 5.4
Homo sapiens Protein: ALG14
Summary
InnateDB Protein IDBP-100393.5
Last Modified 2014-10-13 [Report errors or provide feedback]
Gene Symbol ALG14
Protein Name asparagine-linked glycosylation 14 homolog (S. cerevisiae)
Synonyms
Species Homo sapiens
Ensembl Protein ENSP00000359224
InnateDB Gene IDBG-100391 (ALG14)
Protein Structure
UniProt Annotation
Function May be involved in protein N-glycosylation. May play a role in the second step of the dolichol-linked oligosaccharide pathway. May anchor the catalytic subunit ALG13 to the ER. {ECO:0000269PubMed:16100110}.
Subcellular Localization Endoplasmic reticulum membrane {ECO:0000305}; Single-pass membrane protein {ECO:0000305}.
Disease Associations
Tissue Specificity
Comments
Interactions
Number of Interactions This gene and/or its encoded proteins are associated with 1 experimentally validated interaction(s) in this database.
Experimentally validated
Total 1 [view]
Protein-Protein 1 [view]
Protein-DNA 0
Protein-RNA 0
DNA-DNA 0
RNA-RNA 0
DNA-RNA 0
Gene Ontology

Molecular Function
Accession GO Term
Biological Process
GO:0006488 dolichol-linked oligosaccharide biosynthetic process
GO:0018279 protein N-linked glycosylation via asparagine
GO:0043687 post-translational protein modification
GO:0044267 cellular protein metabolic process
Cellular Component
GO:0005789 endoplasmic reticulum membrane
GO:0016021 integral component of membrane
Protein Structure and Domains
PDB ID
InterPro IPR013969 Oligosaccharide biosynthesis protein Alg14-like
PFAM PF08660
PRINTS
PIRSF
SMART
TIGRFAMs
Post-translational Modifications
Modification
Cross-References
SwissProt Q96F25
PhosphoSite PhosphoSite-Q96F25
TrEMBL
UniProt Splice Variant
Entrez Gene 199857
UniGene Hs.408927
RefSeq NP_659425
HUGO HGNC:28287
OMIM 612866
CCDS CCDS752
HPRD 14466
IMGT
EMBL AK289395 BC011706 CH471097
GenPept AAH11706 BAF82084 EAW73027

If you use InnateDB for your research, please cite the following publication:

Breuer et al., InnateDB: systems biology of innate immunity and beyond - recent updates and continuing curation. Nucl. Acids Res. (2013) 41 (D1) 

InnateDB is being developed jointly by the Brinkman Laboratory (Simon Fraser University, British Columbia, Canada), the Hancock Laboratory (University of British Columbia, Vancouver, British Columbia) and the Lynn EMBL Australia Group (South Australian Health & Medical Research Institute and Flinders University, Adelaide, Australia).

Funding is currently provided by Allergen and EMBL Australia. Previous funding has been provided by Genome Canada, the Foundation for the National Institutes of Health through the Grand Challenges in Global Health initiative and by Teagasc. InnateDB curated interactions are licensed under the Design Science License. All other data is licensed under the terms of the originating database. Contact: innatedb-mail@sfu.ca